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• W1565017492 endingPage "18597" @default.
• W1565017492 startingPage "18589" @default.
• W1565017492 abstract "Activation of many single-transmembrane receptors requires ligand-induced receptor oligomerization. We have examined the oligomerization of the atrial natriuretic peptide receptor, NPR-A, using epitope-tagged receptor in a co-immunoprecipitation assay. Unlike other single-transmembrane receptors, NPR-A oligomerized in a ligand-independent fashion. Extracellular receptor sequences were both necessary and sufficient for oligomer formation. NPR-A was also able to oligomerize with the related natriuretic peptide receptor, NPR-B. A truncated NPR-A lacking most of the cytoplasmic domain blocked activation of the full-length receptor, presumably through formation of an inactive heteromer. These results indicate that oligomerization of this single-transmembrane receptor is important for the transduction of a conformational change across the plasma membrane but are not consistent with models in which natriuretic peptide receptor oligomerization serves merely to bring intracellular domains together." @default.
• W1565017492 created "2016-06-24" @default.
• W1565017492 creator A5010238664 @default.
• W1565017492 creator A5079500025 @default.
• W1565017492 date "1992-09-01" @default.
• W1565017492 modified "2023-09-27" @default.
• W1565017492 title "Ligand-independent oligomerization of natriuretic peptide receptors. Identification of heteromeric receptors and a dominant negative mutant." @default.
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• W1565017492 doi "https://doi.org/10.1016/s0021-9258(19)37002-4" @default.
• W1565017492 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1382057" @default.
• W1565017492 hasPublicationYear "1992" @default.
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